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Press cutting: Sickle cell microcell

12 January 2007

A method to deoxygenate blood's oxygen-carrier, haemoglobin, could lead to treatments for sickle cell anaemia.

Sickle cell haemoglobin (HbS) is different from normal haemoglobin (Hb) by just a single amino acid. This amino acid replacement means that HbS tends to polymerise into long insoluble fibres and it is this that changes the shape of the cell.

"The key to HbS polymerisation is the deoxygenated molecule, as fibre formation occurs only in this state,' said Dr Daren Caruana [UCL Chemistry]. Caruana and colleagues have developed a novel technique for removing oxygen from HbS by electrochemical reduction allowing them to control and study HbS polymerisation in detail. …

"Sickle cell disease is an international health problem affecting millions of people around the world," said Caruana. "This method could not only be used to gain an understanding of the pathophysiology of sickle cell disease, but also as a screening method for drugs that could lead to novel therapeutic strategies for disrupting HbS polymerisation in patients."

Michael Spencelayh, 'Chemical Biology'